Skip Navigation


CIT can broadcast your seminar, conference or meeting live to a world-wide audience over the Internet as a real-time streaming video. The event can be recorded and made available for viewers to watch at their convenience as an on-demand video or a downloadable podcast. CIT can also broadcast NIH-only or HHS-only content.

Membranes, the Flu and in Between

Loading video...

 
   
Air date: Tuesday, August 11, 2009, 11:00:00 AM
Time displayed is Eastern Time, Washington DC Local
Views: Total views: 38 * This only includes stats from October 2011 and forward.
Category: Special
Runtime: 00:59:15
Description: After receiving his Ph.D. from Yale University with Don Engelman and Steve Smith in 1995, Dr. Arkin remained for one year at Yale for postdoctoral training with Axel Brunger. From 1997-2000, Dr. Arkin worked as a Lecturer at the University of Cambridge (UK) before becoming an Associate Professor at the Hebrew University of Jerusalem. He was a visiting scientist at DE Saw Research from 2005-2006, and was promoted to Full Professor at the Hebrew University in 2005. Since 2008, he has been Head of the Life Sciences Institute at the Hebrew University.

Dr. Arkin’s seminar entitled ‘Membranes, the flu and in between’ will cover the following three interrelated topics: The fundamental reason why transmembrane helices are so hydrophobic. Here we show that the reason for their extreme hydrophobicity is not the physical constraints of the lipid bilayer but rather the specificity of the secretion apparatus. How the influenza M2 H+ channel is gated. Here we have unraveled the rotation-based gating of the channel using unbiased restraints from linear and 2D IR spectroscopy. We also present a simple approach to identify new blockers against the channel.

Mechanism of cation specificity of Na+/H+ antiporters. Surprisingly, computational analysis has showed that the Na+ specificity of the pump over K+ does not take place at the binding stage. Experimental data corroborate this conclusion, providing new insight into the how the protein can discriminate between two very similar cations.

The SBIG is a clearinghouse for discussions and interactions between scientists interested in all aspects of molecular structure, from experimental determination by x-ray crystallography, electron microscopy, mass spectrometry, and NMR, to theoretical and computational biology and biophysics, and to the biological application of structural data.

For more information, visit
Structural Biology Interest Group
Debug: Show Debug
NLM Title: Membranes, the flu and in between [electronic resource] / Isaiah Arkin.
Author: Arkin, Isaiah.
National Institutes of Health (U.S.). Structural Biology Interest Group.
Publisher:
Abstract: (CIT): After receiving his Ph.D. from Yale University with Don Engelman and Steve Smith in 1995, Dr. Arkin remained for one year at Yale for postdoctoral training with Axel Brunger. From 1997-2000, Dr. Arkin worked as a Lecturer at the University of Cambridge (UK) before becoming an Associate Professor at the Hebrew University of Jerusalem. He was a visiting scientist at DE Saw Research from 2005-2006, and was promoted to Full Professor at the Hebrew University in 2005. Since 2008, he has been Head of the Life Sciences Institute at the Hebrew University. Dr. Arkin"s seminar entitled "Membranes, the flu and in between" will cover the following three interrelated topics: The fundamental reason why transmembrane helices are so hydrophobic. Here we show that the reason for their extreme hydrophobicity is not the physical constraints of the lipid bilayer but rather the specificity of the secretion apparatus. How the influenza M2 H+ channel is gated. Here we have unraveled the rotation-based gating of the channel using unbiased restraints from linear and 2D IR spectroscopy. We also present a simple approach to identify new blockers against the channel. Mechanism of cation specificity of Na+/H+ antiporters. Surprisingly, computational analysis has showed that the Na+ specificity of the pump over K+ does not take place at the binding stage. Experimental data corroborate this conclusion, providing new insight into the how the protein can discriminate between two very similar cations. The SBIG is a clearinghouse for discussions and interactions between scientists interested in all aspects of molecular structure, from experimental determination by x-ray crystallography, electron microscopy, mass spectrometry, and NMR, to theoretical and computational biology and biophysics, and to the biological application of structural data. For more information, visit Structural Biology Interest Group.
Subjects: Hydrophobic and Hydrophilic Interactions
Ion Channels--physiology
Membrane Potentials--physiology
Protein Transport--physiology
Publication Types: Lectures
Webcasts
Download: To download this event, select one of the available bitrates:
[384k]    How to download a Videocast
NLM Classification: QU 55.7
NLM ID: 101514417
CIT Live ID: 7832
Permanent link: https://videocast.nih.gov/launch.asp?15245